Microglia receptors and their implications in the response to amyloid β for Alzheimer’s disease pathogenesis

Doens, Deborah; Fernández, Patricia L

doi:10.1186/1742-2094-11-48

Cited by 349Neuroinflammation and Neurodegeneration MechanismsAlzheimer's disease research and treatmentsInflammasome and immune disorders

Microglia receptors and their implications in the response to amyloid β for Alzheimer’s disease pathogenesis

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Doens, Deborah, Fernández, Patricia L·2014·Journal of Neuroinflammation

DOI 10.1186/1742-2094-11-48PMC PMC3975152

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Abstract

Alzheimer's disease (AD) is a major public health problem with substantial economic and social impacts around the world. The hallmarks of AD pathogenesis include deposition of amyloid β (Aβ), neurofibrillary tangles, and neuroinflammation. For many years, research has been focused on Aβ accumulation in senile plaques, as these aggregations were perceived as the main cause of the neurodegeneration found in AD. However, increasing evidence suggests that inflammation also plays a critical role in the pathogenesis of AD. Microglia cells are the resident macrophages of the brain and act as the first line of defense in the central nervous system. In AD, microglia play a dual role in disease progression, being essential for clearing Aβ deposits and releasing cytotoxic mediators. Aβ activates microglia through a variety of innate immune receptors expressed on these cells. The mechanisms through which amyloid deposits provoke an inflammatory response are not fully understood, but it is believed that these receptors cooperate in the recognition, internalization, and clearance of Aβ and in cell activation. In this review, we discuss the role of several receptors expressed on microglia in Aβ recognition, uptake, and signaling, and their implications for AD pathogenesis.

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FCγR activation promotes Aβ clearance via phagocytosis.
“FCγR activation also promotes Aβ clearance via phagocytosis [139, 140].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [140]
The Fc receptors section says microglial FcRs mediate Aβ phagocytosis in the presence of antibodies, supporting the proposed clearance pathway. The citing sentence omits that condition; the same section also notes that some antibody-associated Aβ clearance is not FcR-dependent. (LLM, conf=0.84)
Experimental — accuracy not yet measured
Aβ fibrils increase inflammation.
“Aβ fibrils also increase inflammation148 (Fig. 5, purple), which may unanchor residual PDE4A125, and further disinhibit stress signaling pathways.”
From Stress weakens prefrontal networks: molecular insults to higher cognition (2015) · cites this paper as [148]
In mouse macrophages and COS cells, SHIP1 activates the ITIM of the inhibitory receptor FCγRIIβ, which inhibits the activating receptor FCγRIIA to block FCγRIIA-mediated phagocytosis.
“In mouse macrophages and COS cells, SHIP1 was shown to activate the ITIM of the inhibitory receptor FCγRIIβ, which inhibits the activating receptor FCγRIIA to block FCγRIIA-mediated phagocytosis (Fig. 3C).”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [140]
The Fc receptors section (page unavailable) says Fc receptor engagement can activate phagocytosis, but it does not address the claimed inhibitory mechanism. Searches for SHIP1, ITIM, FcγRIIβ, FcγRIIA, and COS cells found no passage describing that mechanism in our copy. (LLM, conf=0.75)
Experimental — accuracy not yet measured
SHIP1 directly inhibits FCγRIIA by binding to its ITAM, which prevents activation of PI3K.
“SHIP1 also was shown to directly inhibit FCγRIIA by binding to its ITAM (Fig. 3C), which prevents the activation of PI3K [134, 137–140].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [140]
The Fc receptors section discusses FcγR signaling in microglia, and the References section lists a study of PI-3 K in that context. Our copy does not address SHIP1 binding the FcγRIIA ITAM or preventing PI3K activation; searches for SHIP1, ITAM, and FcγRIIA found no passage establishing that mechanism. (LLM, conf=0.72)
Experimental — accuracy not yet measured

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Altered intracellular signaling and reduced viability of Alzheimer's disease neuronal cybrids is reproduced by β-amyloid peptide acting through receptor for advanced glycation end products (RAGE)
Onyango, I. G., Tuttle, J. B., & Bennett, J. P. (2005) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.02.012 · Cited by 50 · see citing works
Aβ Potentiates Inflammatory Activation of Glial Cells Induced by Scavenger Receptor Ligands and Inflammatory Mediators in Culture
Murgas, P., Godoy, B., & Rommy von Bernhardi, M. (2012) · Neurotoxicity Research · doi:10.1007/s12640-011-9306-3 · Cited by 49 · see citing works
The formyl peptide receptor like-1 and scavenger receptor MARCO are involved in glial cell activation in bacterial meningitis
Braun, B. J., Slowik, A., Leib, S. L., Lucius, R., Varoga, D. J., Wruck, C. J., Jansen, S., Podschun, R., Pufe, T., & Brandenburg, L. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-11 · Cited by 48 · see citing works
Novel pathophysiological role of classical chemotactic peptide receptors and their communications with chemokine receptors
Le, Y., Li, B., Gong, W., Shen, W., Hu, J., Dunlop, N. M., Oppenheim, J. J., & Wang, J. (2000) · Immunological Reviews · doi:10.1034/j.1600-065x.2000.17704.x · Cited by 47 · see citing works
Scavenger receptors: Implications in atherothrombotic disorders
Ashraf, M. Z., & Gupta, N. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.01.019 · Cited by 44 · see citing works
Complement activation fragment C5a receptors, CD88 and C5L2, are associated with neurofibrillary pathology
Fonseca, M. I., McGuire, S. O., Counts, S., & Tenner, A. J. (2013) · Journal of Neuroinflammation · doi:10.1186/1742-2094-10-25 · Cited by 43 · see citing works
Immunoglobulin G Fc receptor deficiency prevents Alzheimer-like pathology and cognitive impairment in mice
Fernández‐Vizarra, P., López‐Franco, Ó., Mallavia, B., Higuera‐Matas, A., López-Parra, V., Ortiz-Muñoz, G., Ambrosio, E., Egido, J., Almeida, O. F. X., & Gómez‐Guerrero, C. (2012) · Brain · doi:10.1093/brain/aws195 · Cited by 42 · see citing works
The Interaction of Amyloid β and the Receptor for Advanced Glycation Endproducts Induces Matrix Metalloproteinase-2 Expression in Brain Endothelial Cells
Du, H., Li, P., Wang, J., Qing, X., & Li, W. (2011) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-011-9744-8 · Cited by 40 · see citing works
Identification of functional domains in the formyl peptide receptor‐like 1 for agonist‐induced cell chemotaxis
Le, Y., Ye, R. D., Gong, W., Li, J., Iribarren, P., & Wang, J. M. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2004.04514.x · Cited by 39 · see citing works
Potential Immunotargets for Alzheimer's Disease Treatment Strategies
Fernández, P. L., Britton, G. B., & Rao, K. S. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121222 · Cited by 37 · see citing works
Self-citation
Induction of the Formyl Peptide Receptor 2 in Microglia by IFN-γ and Synergy with CD40 Ligand
Chen, K., Iribarren, P., Huang, J., Zhang, L., Gong, W., Cho, E. H., Lockett, S., Dunlop, N. M., & Wang, J. M. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.3.1759 · Cited by 36 · see citing works
Complement receptor 3 (CD11b/CD18) is implicated in the elimination of β-amyloid peptides
Choucair‐Jaafar, N., Laporte, V., Levy, R., Poindron, P., Lombard, Y., & Gies, J. (2010) · Fundamental and Clinical Pharmacology · doi:10.1111/j.1472-8206.2010.00811.x · Cited by 35 · see citing works
Scavenger receptor class A ligands induce secretion of IL1β and exert a modulatory effect on the inflammatory activation of astrocytes in culture
Godoy, B., Murgas, P., Tichauer, J. E., & Rommy von Bernhardi, M. (2012) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2012.06.004 · Cited by 34 · see citing works
The Interaction of Amyloid b and the Receptor for Advanced Glycation Endproducts Induces Matrix Metalloproteinase-2 Expression in Brain Endothelial Cells
DuPengtao, H., Wang, L., & Li, X. Q. (2012) · Cited by 34 · see citing works
Platelet activation and inhibition of malarial cytoadherence by the anti-CD36 IgM monoclonal antibody NL07
Alessio, M., Greco, N., Primo, L., Ghigo, D., Bosìa, A., Tandon, N., Ockenhouse, C., Jamieson, G., & Malavasi, F. (1993) · Blood · doi:10.1182/blood.v82.12.3637.3637 · Cited by 27 · see citing works
Intra-Blood-Brain-Barrier Synthesis of Immunoglobulins in Patients with Dementia of the Alzheimer Type
Blennow, K., Wallin, A., Davidsson, P., Fredman, P., Gottfries, C., & Svennerholm, L. T. (1990) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-199004020-00002 · Cited by 24 · see citing works
Stereotaxic Injection of IgG From Patients With Alzheimer Disease Initiates Injury of Cholinergic Neurons of the Basal Forebrain
Engelhardt, J. I., Le, W.-D., Siklós, L., Obál, I., Boda, K., & Appel, S. H. (2000) · Archives of Neurology · doi:10.1001/archneur.57.5.681 · Cited by 19 · see citing works
Intra-Blood-Brain-Barrier Synthesis of Immunoglobulins in Patients with Dementia of the Alzheimer Type
Blennow, K., Wallin, A., Davidsson, P., et al. (1990) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-199040200-00002 · Cited by 19 · see citing works
Central Nervous System IgG Synthesis Rates in Alzheimer Disease
Small, G. W., Rosenthal, M. J., & Tourtellotte, W. W. (1994) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-199408010-00006 · Cited by 12 · see citing works
Induction of MC-1 immunoreactivity in axons after injection of the Fc fragment of human immunoglobulins in macaque monkeys
Bouras, C., Riederer, B. M., Hof, P. R., & Giannakopoulos, P. (2003) · Acta Neuropathologica · doi:10.1007/s00401-002-0617-6 · Cited by 9 · see citing works

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Neuroinflammation and microglial activation in Alzheimer disease: where do we go from here?
Leng, F., & Edison, P. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-020-00435-y · Cited by 3,179 · see citing works
The Gut Microbiota and Alzheimer’s Disease
Jiang, C., Li, G., Huang, P., Liu, Z., & Zhao, B. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161141 · Cited by 852 · see citing works
TREM2 Is a Receptor for β-Amyloid that Mediates Microglial Function
Zhao, Y., Wu, X., Li, X., Jiang, L.-L., Gui, X., Liu, Y., Sun, Y., Zhu, B., Piña-Crespo, J. C., Zhang, M., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.031 · Cited by 763 · see citing works
Stress weakens prefrontal networks: molecular insults to higher cognition
Arnsten, A. F. T. (2015) · Nature Neuroscience · doi:10.1038/nn.4087 · Cited by 752 · see citing works
Markers of microglia in post-mortem brain samples from patients with Alzheimer’s disease: a systematic review
Hopperton, K. E., Mohammad, D., Trépanier, M. O., Giuliano, V, & Bazinet, R. P. (2018) · Molecular Psychiatry · doi:10.1038/mp.2017.246 · Cited by 567 · see citing works
Mechanisms of Aβ Clearance and Degradation by Glial Cells
Ries, M., & Sastre, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00160 · Cited by 527 · see citing works
“The degree of involvement of Fc receptors in the clearance of Aβ bound by endogenous antibodies such as IgGs is currently not well elucidated (Doens and Fernández, 2014).”
Background
LC3-Associated Endocytosis Facilitates β-Amyloid Clearance and Mitigates Neurodegeneration in Murine Alzheimer’s Disease
Heckmann, B. L., Teubner, B. J. W., Tummers, B., Boada-Romero, E., Harris, L., Yang, M., Guy, C. S., Zakharenko, S. S., & Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.05.056 · Cited by 503 · see citing works
“…toll-like receptors (TLRs) (Gurley et al., 2008), Fc receptors (Fuller et al., 2014), Ig-superfamily receptors including TREM2 (Ulrich et al., 2014; Wang et al., 2016; Zhao et al., 2018), scavenger receptors (SR) (Wilkinson and El Khoury, 2012) and complement receptors (Doens and Fernandez, 2014).”
Influential
Effect of Chronic Oxidative Stress on Neuroinflammatory Response Mediated by CD4+T Cells in Neurodegenerative Diseases
Solleiro-Villavicencio, H., & Rivas-Arancibia, S. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00114 · Cited by 463 · see citing works
Alzheimer’s disease: insights into pathology, molecular mechanisms, and therapy
Zheng, Q., & Wang, X. (2024) · Protein & Cell · doi:10.1093/procel/pwae026 · Cited by 454 · see citing works
An early and late peak in microglial activation in Alzheimer’s disease trajectory
Fan, Z., Brooks, D. J., Okello, A., & Edison, P. (2017) · Brain · doi:10.1093/brain/aww349 · Cited by 422 · see citing works
Lipopolysaccharide-Induced Model of Neuroinflammation: Mechanisms of Action, Research Application and Future Directions for Its Use
Skrzypczak-Wiercioch, A., & Sałat, K. (2022) · Molecules · doi:10.3390/molecules27175481 · Cited by 406 · see citing works
Microglia-Mediated Synapse Loss in Alzheimer's Disease
Rajendran, L., & Paolicelli, R. C. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.1136-17.2017 · Cited by 355 · see citing works
Neuroinflammation after intracerebral hemorrhage
Mracsko, E. Z., & Veltkamp, R. C. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00388 · Cited by 343 · see citing works
Microglia Phenotypes in Aging and Neurodegenerative Diseases
Wendimu, M. Y., & Hooks, S. B. (2022) · Cells · doi:10.3390/cells11132091 · Cited by 336 · see citing works
Gut microbiota in neurodegenerative disorders
Sarkar, S. R., & Banerjee, S. (2019) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2019.01.004 · Cited by 319 · see citing works
Proteinopathy, oxidative stress and mitochondrial dysfunction: cross talk in Alzheimer's disease and Parkinson's disease
Ganguly, G., Chakrabarti, S., Chatterjee, U., & Saso, L. (2017) · Drug Design Development and Therapy · doi:10.2147/dddt.s130514 · Cited by 295 · see citing works
Alzheimer's disease and type 2 diabetes: a critical assessment of the shared pathological traits
Chatterjee, S., & Mudher, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00383 · Cited by 270 · see citing works
Amyloid-β Receptors: The Good, the Bad, and the Prion Protein
Jarosz-Griffiths, H. H., Noble, E., Rushworth, J. V., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.702704 · Cited by 256 · see citing works
Lipid and Lipoprotein Metabolism in Microglia
Loving, B. A., & Bruce, K. D. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00393 · Cited by 255 · see citing works
Microglia and Alzheimer’s Disease
Merighi, S., Nigro, M., Travagli, A., & Gessi, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112990 · Cited by 236 · see citing works
Characterizing newly repopulated microglia in the adult mouse: impacts on animal behavior, cell morphology, and neuroinflammation
Elmore, M. R. P., Lee, R. J., West, B. L., & Green, K. N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122912 · Cited by 228 · see citing works
Anti-Inflammatory Targets for the Treatment of Reperfusion Injury in Stroke
Mizuma, A., & Yenari, M. A. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00467 · Cited by 226 · see citing works
The microglial ATP‐gated ion channel P2X7 as a CNS drug target
Bhattacharya, A., & Biber, K. (2016) · Glia · doi:10.1002/glia.23001 · Cited by 221 · see citing works
Automated Morphological Analysis of Microglia After Stroke
Heindl, S., Gesierich, B. G., Benakis, C., Llovera, G., Duering, M., & Liesz, A. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00106 · Cited by 220 · see citing works
Therapeutic B-cell depletion reverses progression of Alzheimer’s disease
Kim, K., Wang, X., Ragonnaud, E., Bodogai, M., Illouz, T., DeLuca, M., McDevitt, R. A., Gusev, F., Okun, E., Rogaev, E., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22479-4 · Cited by 206 · see citing works
Inflammation context in Alzheimer’s disease, a relationship intricate to define
Novoa, C., Salazar, P., Cisternas, P., Gherardelli, C., Vera-Salazar, R., Zolezzi, J. M., & Inestrosa, N. C. (2022) · Biological Research · doi:10.1186/s40659-022-00404-3 · Cited by 206 · see citing works
Neuroinflammation and neurogenesis in Alzheimer's disease and potential therapeutic approaches
Sung, P.-S., Lin, P.-Y., Liu, C.-H., Su, H.-C., & Tsai, K.-J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030701 · Cited by 193 · see citing works
β-Amyloid Clustering around ASC Fibrils Boosts Its Toxicity in Microglia
Friker, L. L., Scheiblich, H., Hochheiser, I. V., Brinkschulte, R., Riedel, D., Latz, E., Geyer, M., & Heneka, M. T. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.025 · Cited by 191 · see citing works
Alzheimer's disease and type 2 diabetes mellitus are distinct diseases with potential overlapping metabolic dysfunction upstream of observed cognitive decline
Chornenkyy, Y., Wang, W., Wei, A. L., & Nelson, P. T. (2018) · Brain Pathology · doi:10.1111/bpa.12655 · Cited by 184 · see citing works
Microglia and lipids: how metabolism controls brain innate immunity
Chausse, B., Kakimoto, P. A., & Kann, O. (2021) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2020.08.001 · Cited by 181 · see citing works
Mitochondrial Dysfunction and Alzheimer’s Disease: Role of Microglia
Agrawal, I., & Jha, S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00252 · Cited by 181 · see citing works
Epigallocatechin-3-Gallate (EGCG): New Therapeutic Perspectives for Neuroprotection, Aging, and Neuroinflammation for the Modern Age
Payne, A., Nahashon, S. N., Taka, E., Adinew, G. M., & Soliman, K. F. A. (2022) · Biomolecules · doi:10.3390/biom12030371 · Cited by 171 · see citing works
Molecular Mechanisms of Neuroinflammation in Aging and Alzheimer’s Disease Progression
Andronie-Cioară, F. L., Ardelean, A. I., Nistor-Cseppento, C. D., Jurcău, A., Jurcău, M. C., Pașcalău, N., & Marcu, F. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031869 · Cited by 164 · see citing works
Protective Effect of Amyloid-β Peptides Against Herpes Simplex Virus-1 Infection in a Neuronal Cell Culture Model
Bourgade, K., Le Page, A., Bocti, C., Witkowski, J. M., Dupuis, G., Frost, E. H., & Fülöp, T. (2016) · Journal of Alzheimer’s Disease · doi:10.3233/jad-150652 · Cited by 161 · see citing works
Alzheimer’s Disease Pathogenesis: Role of Autophagy and Mitophagy Focusing in Microglia
Eshraghi, M., Adlimoghaddam, A., Mahmoodzadeh, A., Sharifzad, F., Yasavoli-Sharahi, H., Lorzadeh, S., Albensi, B. C., & Ghavami, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073330 · Cited by 158 · see citing works
Deacetylation of TFEB promotes fibrillar Aβ degradation by upregulating lysosomal biogenesis in microglia
Bao, J., Zheng, L., Zhang, Q., Li, X., Zhang, X., Li, Z., Bai, X., Zhang, Z., Huo, W., Zhao, X., et al. (2016) · Protein & Cell · doi:10.1007/s13238-016-0269-2 · Cited by 157 · see citing works
Inhibition of REV‐ERBs stimulates microglial amyloid‐beta clearance and reduces amyloid plaque deposition in the 5XFAD mouse model of Alzheimer’s disease
Lee, J., Kim, D. E., Griffin, P. Y., Sheehan, P. W., Kim, D., Musiek, E. S., & Yoon, S. (2019) · Aging Cell · doi:10.1111/acel.13078 · Cited by 156 · see citing works
Neuroinflammatory Processes, A1 Astrocyte Activation and Protein Aggregation in the Retina of Alzheimer’s Disease Patients, Possible Biomarkers for Early Diagnosis
Grimaldi, A., Pediconi, N., Oieni, F., Pizzarelli, R., Rosito, M., Giubettini, M., Santini, T., Limatola, C., Ruocco, G., Ragozzino, D., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00925 · Cited by 153 · see citing works
Dysregulated phosphoinositide 3-kinase signaling in microglia: shaping chronic neuroinflammation
Chu, E., Mychasiuk, R., Hibbs, M. L., & Semple, B. D. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02325-6 · Cited by 152 · see citing works
Microglial dysfunction connects depression and Alzheimer’s disease
Santos, L. E., Beckman, D., & Ferreira, S. T. (2016) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2015.11.011 · Cited by 119 · see citing works
Chalcone and its analogs: Therapeutic and diagnostic applications in Alzheimer’s disease
Thapa, P., Upadhyay, S. P., Suo, W. Z., Singh, V., Gurung, P., Lee, E. S., Sharma, R., & Sharma, M. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104681 · Cited by 147 · see citing works
The relationship between iron dyshomeostasis and amyloidogenesis in Alzheimer's disease: Two sides of the same coin
Peters, D. G., Connor, J. R., & Meadowcroft, M. D. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.08.007 · Cited by 145 · see citing works
Microglia at center stage: a comprehensive review about the versatile and unique residential macrophages of the central nervous system
Lannes, N., Eppler, E., Etemad, S., Yotovski, P., & Filgueira, L. (2017) · Oncotarget · doi:10.18632/oncotarget.23106 · Cited by 139 · see citing works
Exosomes from NSC-34 Cells Transfected with hSOD1-G93A Are Enriched in miR-124 and Drive Alterations in Microglia Phenotype
Pinto, S., Cunha, C., Barbosa, M., Vaz, A. R., & Brites, D. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00273 · Cited by 135 · see citing works
GWAS of longitudinal amyloid accumulation on18F-florbetapir PET in Alzheimer’s disease implicates microglial activation geneIL1RAP
Ramanan, V. K., Risacher, S. L., Nho, K., Kim, S., Shen, L., McDonald, B. C., Yoder, K. K., Hutchins, G. D., West, J. D., Tallman, E. F., et al. (2015) · Brain · doi:10.1093/brain/awv231 · Cited by 133 · see citing works
Microglial mTOR Activation Upregulates Trem2 and Enhances β-Amyloid Plaque Clearance in the 5XFAD Alzheimer's Disease Model
Shi, Q., Chang, C., Saliba, A., & Bhat, M. A. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.2427-21.2022 · Cited by 134 · see citing works
Phenotypic clustering: a novel method for microglial morphology analysis
Verdonk, F., Roux, P., Flamant, P., Fiette, L., Bozza, F. A., Simard, S., Lemaire, M., Plaud, B., Shorte, S. L., Sharshar, T., et al. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0614-7 · Cited by 132 · see citing works
Microglia in Alzheimer’s Disease in the Context of Tau Pathology
Perea, J. R., Bolós, M., & Ávila, J. (2020) · Biomolecules · doi:10.3390/biom10101439 · Cited by 127 · see citing works
The Crucial Role of the Blood–Brain Barrier in Neurodegenerative Diseases: Mechanisms of Disruption and Therapeutic Implications
Kim, S., Jung, U. J., & Kim, S. R. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14020386 · Cited by 123 · see citing works
Inflammatory mechanisms in neurodegeneration
Nichols, M. R., St‐Pierre, M., Wendeln, A., Makoni, N. J., Gouwens, L. K., Garrad, E. C., Sohrabi, M., Neher, J. J., Tremblay, M., & Combs, C. K. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14674 · Cited by 122 · see citing works
The role of innate immunity in Alzheimer's disease
Ennerfelt, H. E., & Lukens, J. R. (2020) · Immunological Reviews · doi:10.1111/imr.12896 · Cited by 121 · see citing works
Ultrastructural evidence of microglial heterogeneity in Alzheimer’s disease amyloid pathology
El Hajj, H., Savage, J. C., Bisht, K., Parent, M., Vallières, L., Rivest, S., & Tremblay, M.-È. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1473-9 · Cited by 119 · see citing works
Sex differences in the phagocytic and migratory activity of microglia and their impairment by palmitic acid
Yanguas‐Casás, N., Crespo‐Castrillo, A., CEBALLOS, M. L. D., Chowen, J. A., Azcoitia, Í., Arévalo, M., & García‐Segura, L. M. (2017) · Glia · doi:10.1002/glia.23263 · Cited by 116 · see citing works
Noncanonical function of an autophagy protein prevents spontaneous Alzheimer’s disease
Heckmann, B. L., Teubner, B. J. W., Boada-Romero, E., Tummers, B., Guy, C., Fitzgerald, P., Mayer, U., Carding, S., Zakharenko, S. S., Wileman, T., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb9036 · Cited by 114 · see citing works
Reduced basal forebrain atrophy progression in a randomized Donepezil trial in prodromal Alzheimer’s disease
Cavedo, E., Grothe, M. J., Colliot, O., Lista, S., Marie Chupin, A., Dormont, D., Houot, M., Lehéricy, S., Teipel, S. J., Dubois, B., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-09780-3 · Cited by 109 · see citing works
Drug repositioning for Alzheimer’s disease based on systematic “omics” data mining
Zhang, M., Schmitt-Ulms, G., Sato, C., Xi, Z., Zhang, Y., Zhou, Y., St George-Hyslop, P., & Rogaeva, E. (2016) · PLOS ONE · doi:10.1371/journal.pone.0168812 · Cited by 108 · see citing works
Role of α-synuclein in microglia: autophagy and phagocytosis balance neuroinflammation in Parkinson’s disease
Lv, Q.-K., Tao, K., Wang, X.-B., Yao, X., Pang, M., Liu, J., Wang, F., & Liu, C. (2023) · Inflammation Research · doi:10.1007/s00011-022-01676-x · Cited by 108 · see citing works
Anti CD163+, Iba1+, and CD68+ Cells in the Adult Human Inner Ear
O’Malley, J. T., Nadol, J. B., & McKenna, M. J. (2015) · Otology & Neurotology · doi:10.1097/mao.0000000000000879 · Cited by 105 · see citing works
The Use of Ginkgo Biloba L. as a Neuroprotective Agent in the Alzheimer’s Disease
Nowak, A., Kojder, K., Zielonka-Brzezicka, J., Wróbel, J., Bosiacki, M., Fabiańska, M., Wróbel, M., Sołek-Pastuszka, J., & Klimowicz, A. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.775034 · Cited by 105 · see citing works
Microglia-targeting nanotherapeutics for neurodegenerative diseases
Zhao, N., Francis, N. L., Calvelli, H. R., & Moghe, P. V. (2020) · APL Bioengineering · doi:10.1063/5.0013178 · Cited by 104 · see citing works
Alzheimer’s Disease: Mechanism and Approach to Cell Therapy
Amemori, T., Jendelová, P., Růžička, J., Urdzíková, L. M., & Syková, E. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161125961 · Cited by 102 · see citing works
Prevention of C5aR1 signaling delays microglial inflammatory polarization, favors clearance pathways and suppresses cognitive loss
Hernandez, M. X., Jiang, S., Cole, T. A., Chu, S., Fonseca, M. I., Fang, M. J., Hohsfield, L. A., Torres, M. D., Green, K. N., Wetsel, R. A., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0210-z · Cited by 101 · see citing works
Amphiphilic Distyrylbenzene Derivatives as Potential Therapeutic and Imaging Agents for Soluble and Insoluble Amyloid β Aggregates in Alzheimer’s Disease
Sun, L., Cho, H.-J., Sen, S., Arango, A. S., Huynh, T. T., Huang, Y., Bandara, N., Rogers, B. E., Tajkhorshid, E., & Mirica, L. M. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c05470 · Cited by 100 · see citing works
Neuroprotective Effects of Aged Garlic Extract on Cognitive Dysfunction and Neuroinflammation Induced by β-Amyloid in Rats
Nillert, N., Pannangrong, W., Welbat, J. U., Chaijaroonkhanarak, W., Sripanidkulchai, K., & Sripanidkulchai, B. (2017) · Nutrients · doi:10.3390/nu9010024 · Cited by 99 · see citing works
Type 2 Diabetes Mellitus as a Risk Factor for Alzheimer’s Disease: Review and Meta-Analysis
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Authors: Doens, D., & Fernández, P. L.
Affiliations: Acharya Nagarjuna University (IN)
Instituto de Investigaciones Científicas y Servicios de Alta Tecnología (PA)
Corresponding author: Fernández, Patricia L
ORCID: Fernández, Patricia L
Venue: Journal of Neuroinflammation
Publisher: Springer Science and Business Media LLC
Published: 2014
Volume: 11
Issue: 1
Pages: 48
ISSN: 1742-2094 (ISSN-L)
DOI: 10.1186/1742-2094-11-48
PMC: PMC3975152
OpenAlex: W2100011299
Cited by: 348
References: 172
Citations by year: 2026: 22 · 2025: 42 · 2024: 33 · 2023: 33 · 2022: 36 · 2021: 27 · 2020: 24 · 2019: 24 · 2018: 27 · 2017: 26 · 2016: 24 · 2015: 25 · 2014: 5
FWCI: 2.16
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Journal of Neuroinflammation (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Greater South Information System
Topics: Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Keywords: Alzheimer's disease, amyloid-beta, microglia, innate immune receptors, neuroinflammation, amyloid clearance, receptor signaling, microglial activation, amyloid plaques, neurodegeneration
MeSH terms: Alzheimer Disease, Animals, Humans, Receptors, Immunologic, Amyloid beta-Peptides, Microglia

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Microglia receptors and their implications in the response to amyloid β for Alzheimer’s disease pathogenesis

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